Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2014 (2014), Article ID 641979, 11 pages
http://dx.doi.org/10.1155/2014/641979
Review Article

Dysregulation of Histone Acetyltransferases and Deacetylases in Cardiovascular Diseases

1Cardiovascular Center, The First Hospital of Jilin University, 71 Xinmin Street, Changchun 130021, China
2Department of Pediatrics, Kosair Children Hospital Research Institute, University of Louisville, 570 South Preston Street, Baxter I, Suite 304F, Louisville, KY 40202, USA
3The Second Hospital of Jilin University, Changchun 130041, China
4The Second Artillery General Hospital, Beijing 100088, China

Received 16 October 2013; Accepted 6 January 2014; Published 18 February 2014

Academic Editor: José Luís García-Giménez

Copyright © 2014 Yonggang Wang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. N. Cohn, R. Ferrari, and N. Sharpe, “Cardiac remodeling—concepts and clinical implications: a consensus paper from an international forum on cardiac remodeling,” Journal of the American College of Cardiology, vol. 35, no. 3, pp. 569–582, 2000. View at Publisher · View at Google Scholar · View at Scopus
  2. M. P. Gupta, S. A. Samant, S. H. Smith, and S. G. Shroff, “HDAC4 and PCAF bind to cardiac sarcomeres and play a role in regulating myofilament contractile activity,” The Journal of Biological Chemistry, vol. 283, no. 15, pp. 10135–10146, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. S. A. Samant, D. S. Courson, N. R. Sundaresan et al., “HDAC3-dependent reversible lysine acetylation of cardiac myosin heavy chain isoforms modulates their enzymatic and motor activity,” The Journal of Biological Chemistry, vol. 286, no. 7, pp. 5567–5577, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. V. G. Sharov, H. N. Sabbah, H. Shimoyama, A. V. Goussev, M. Lesch, and S. Goldstein, “Evidence of cardiocyte apoptosis in myocardium of dogs with chronic heart failure,” The American Journal of Pathology, vol. 148, no. 1, pp. 141–149, 1996. View at Google Scholar · View at Scopus
  5. K. T. Weber, R. Pick, M. A. Silver et al., “Fibrillar collagen and remodeling of dilated canine left ventricle,” Circulation, vol. 82, no. 4, pp. 1387–1401, 1990. View at Google Scholar · View at Scopus
  6. A. Iyer, A. Fenning, J. Lim et al., “Antifibrotic activity of an inhibitor of histone deacetylases in DOCA-salt hypertensive rats,” British Journal of Pharmacology, vol. 159, no. 7, pp. 1408–1417, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. H. J. Kee, I. S. Sohn, K. I. Nam et al., “Inhibition of histone deacetylation blocks cardiac hypertrophy induced by angiotensin II infusion and aortic banding,” Circulation, vol. 113, no. 1, pp. 51–59, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. S. Jain, J. Wei, L. R. Mitrani, and N. H. Bishopric, “Auto-acetylation stabilizes p300 in cardiac myocytes during acute oxidative stress, promoting STAT3 accumulation and cell survival,” Breast Cancer Research and Treatment, vol. 135, no. 1, pp. 103–114, 2012. View at Publisher · View at Google Scholar · View at Scopus
  9. D. J. Cao, Z. V. Wang, P. K. Battiprolu et al., “Histone deacetylase (HDAC) inhibitors attenuate cardiac hypertrophy by suppressing autophagy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 10, pp. 4123–4128, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. T. A. McKinsey, “Targeting inflammation in heart failure with histone deacetylase inhibitors,” Molecular Medicine, vol. 17, no. 5-6, pp. 434–441, 2011. View at Publisher · View at Google Scholar · View at Scopus
  11. R. L. Montgomery, M. J. Potthoff, M. Haberland et al., “Maintenance of cardiac energy metabolism by histone deacetylase 3 in mice,” The Journal of Clinical Investigation, vol. 118, no. 11, pp. 3588–3597, 2008. View at Publisher · View at Google Scholar · View at Scopus
  12. S. L. Berger, T. Kouzarides, R. Shiekhattar, and A. Shilatifard, “An operational definition of epigenetics,” Genes & Development, vol. 23, no. 7, pp. 781–783, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. H. A. Lee, D. Y. Lee, H. M. Cho et al., “Histone deacetylase inhibition attenuates transcriptional activity of mineralocorticoid receptor through its acetylation and prevents development of hypertension,” Circulation Research, vol. 112, no. 7, pp. 1004–1012, 2013. View at Publisher · View at Google Scholar
  14. S. Y. Mu, T. Shimosawa, S. Ogura et al., “Epigenetic modulation of the renal β-adrenergic–WNK4 pathway in salt-sensitive hypertension,” Nature Medicine, vol. 17, no. 5, pp. 573–580, 2011. View at Publisher · View at Google Scholar
  15. S. S. Vadvalkar, C. N. Baily, S. Matsuzaki et al., “Metabolic inflexibility and protein lysine acetylation in heart mitochondria of a chronic model of Type 1 diabetes,” The Biochemical Journal, vol. 449, no. 1, pp. 253–261, 2013. View at Publisher · View at Google Scholar
  16. M. A. Thal, P. Krishnamurthy, A. R. Mackie et al., “Enhanced angiogenic and cardiomyocyte differentiation capacity of epigenetically reprogrammed mouse and human endothelial progenitor cells augments their efficacy for ischemic myocardial repair,” Circulation Research, vol. 111, no. 2, pp. 180–190, 2012. View at Publisher · View at Google Scholar
  17. F. Soubrier, W. K. Chung, R. Machado et al., “Genetics and genomics of pulmonary arterial hypertension,” Journal of the American College of Cardiology, vol. 62, no. 25, supplement, pp. D13–D21, 2013. View at Publisher · View at Google Scholar
  18. Q. Yang, Z. Lu, R. Ramchandran et al., “Pulmonary artery smooth muscle cell proliferation and migration in fetal lambs acclimatized to high-altitude long-term hypoxia: role of histone acetylation,” American Journal of Physiology, vol. 303, no. 11, pp. L1001–L1010, 2012. View at Publisher · View at Google Scholar
  19. Y. Tang, J. M. Boucher, and L. Liaw, “Histone deacetylase activity selectively regulates notch-mediated smooth muscle differentiation in human vascular cells,” Journal of the American Heart Association, vol. 1, no. 3, Article ID e000901, 2012. View at Publisher · View at Google Scholar
  20. Y. Liu, Z. Wang, J. Wang et al., “A histone deacetylase inhibitor, largazole, decreases liver fibrosis and angiogenesis by inhibiting transforming growth factor-β and vascular endothelial growth factor signalling,” Liver International, vol. 33, no. 4, pp. 504–515, 2013. View at Publisher · View at Google Scholar
  21. V. G. Allfrey, B. G. T. Pogo, V. C. Littau, E. L. Gershey, and A. E. Mirsky, “Histone acetylation in insect chromosomes,” Science, vol. 159, no. 3812, pp. 314–316, 1968. View at Google Scholar · View at Scopus
  22. X.-J. Yang and E. Seto, “Lysine acetylation: codified crosstalk with other posttranslational modifications,” Molecular Cell, vol. 31, no. 4, pp. 449–461, 2008. View at Publisher · View at Google Scholar · View at Scopus
  23. G. Blander and L. Guarente, “The Sir2 family of protein deacetylases,” Annual Review of Biochemistry, vol. 73, pp. 417–435, 2004. View at Publisher · View at Google Scholar · View at Scopus
  24. W. L. Cheung, S. D. Briggs, and C. D. Allis, “Acetylation and chromosomal functions,” Current Opinion in Cell Biology, vol. 12, no. 3, pp. 326–333, 2000. View at Publisher · View at Google Scholar · View at Scopus
  25. X.-J. Yang and E. Seto, “HATs and HDACs: from structure, function and regulation to novel strategies for therapy and prevention,” Oncogene, vol. 26, no. 37, pp. 5310–5318, 2007. View at Publisher · View at Google Scholar · View at Scopus
  26. Y. S. Kim, M. J. Kim, T. H. Koo et al., “Histone deacetylase is required for the activation of Wnt/β-catenin signaling crucial for heart valve formation in zebrafish embryos,” Biochemical and Biophysical Research Communications, vol. 423, no. 1, pp. 140–146, 2012. View at Publisher · View at Google Scholar
  27. C. E. Brown, T. Lechner, L. Howe, and J. L. Workman, “The many HATs of transcription coactivators,” Trends in Biochemical Sciences, vol. 25, no. 1, pp. 15–19, 2000. View at Publisher · View at Google Scholar · View at Scopus
  28. M. R. Parthun, J. Widom, and D. E. Gottschling, “The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism,” Cell, vol. 87, no. 1, pp. 85–94, 1996. View at Publisher · View at Google Scholar · View at Scopus
  29. R. J. Burgess, H. Zhou, J. Han, and Z. Zhang, “A role for Gcn5 in replication-coupled nucleosome assembly,” Molecular Cell, vol. 37, no. 4, pp. 469–480, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. A. R. Sklenar and M. R. Parthun, “Characterization of yeast histone H3-specific type B histone acetyltransferases identifies an ADA2-independent Gcn5p activity,” BMC Biochemistry, vol. 5, article 11, 2004. View at Publisher · View at Google Scholar
  31. X. Yang, W. Yu, L. Shi et al., “HAT4, a golgi apparatus-anchored B-type histone acetyltransferase, acetylates free histone H4 and facilitates chromatin assembly,” Molecular Cell, vol. 44, no. 1, pp. 39–50, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. T.-P. Yao, S. P. Oh, M. Fuchs et al., “Gene dosage-dependent embryonic development and proliferation defects in mice lacking the transcriptional integrator p300,” Cell, vol. 93, no. 3, pp. 361–372, 1998. View at Publisher · View at Google Scholar · View at Scopus
  33. N. Shikama, W. Lutz, R. Kretzschmar et al., “Essential function of p300 acetyltransferase activity in heart, lung and small intestine formation,” The EMBO Journal, vol. 22, no. 19, pp. 5175–5185, 2003. View at Publisher · View at Google Scholar · View at Scopus
  34. G. Majumdar, P. Adris, N. Bhargava et al., “Pan-histone deacetylase inhibitors regulate signaling pathways involved in proliferative and pro-inflammatory mechanisms in H9c2 cells,” BMC Genomics, vol. 13, article 709, 2012. View at Publisher · View at Google Scholar
  35. L. Zhang, X. Qin, Y. Zhao et al., “Inhibition of histone deacetylases preserves myocardial performance and prevents cardiac remodeling through stimulation of endogenous angiomyogenesis,” The Journal of Pharmacology and Experimental Therapeutics, vol. 341, no. 1, pp. 285–293, 2012. View at Publisher · View at Google Scholar · View at Scopus
  36. D. Mosashvilli, P. Kahl, C. Mertens et al., “Global histone acetylation levels: prognostic relevance in patients with renal cell carcinoma,” Cancer Science, vol. 101, no. 12, pp. 2664–2669, 2010. View at Publisher · View at Google Scholar · View at Scopus
  37. S. E. Elsheikh, A. R. Green, E. A. Rakha et al., “Global histone modifications in breast cancer correlate with tumor phenotypes, prognostic factors, and patient outcome,” Cancer Research, vol. 69, no. 9, pp. 3802–3809, 2009. View at Publisher · View at Google Scholar · View at Scopus
  38. S. Ceccatelli, R. Bose, K. Edoff et al., “Long-lasting neurotoxic effects of exposure to methylmercury during development,” Journal of Internal Medicine, vol. 273, no. 5, pp. 490–497, 2013. View at Publisher · View at Google Scholar
  39. K. N. McFarland, S. Das, T. T. Sun et al., “Genome-wide histone acetylation is altered in a transgenic mouse model of Huntington's disease,” PloS ONE, vol. 7, no. 7, Article ID e41423, 2012. View at Publisher · View at Google Scholar
  40. R. E. Norman, D. O. Carpenter, J. Scott et al., “Environmental exposures: an underrecognized contribution to noncommunicable diseases,” Reviews on Environmental Health, vol. 28, no. 1, pp. 59–65, 2013. View at Publisher · View at Google Scholar
  41. Q. Xu, X. Lin, L. Andrews et al., “Histone deacetylase inhibition reduces cardiac connexin43 expression and gap junction communication,” Frontiers in Pharmacology, vol. 4, article 44, 2013. View at Publisher · View at Google Scholar
  42. M. Xie and J. A. Hill, “HDAC-dependent ventricular remodeling,” Trends in Cardiovascular Medicine, vol. 23, no. 6, pp. 229–235, 2013. View at Publisher · View at Google Scholar
  43. J. P. Cardinale, S. Sriramula, R. Pariaut et al., “HDAC inhibition attenuates inflammatory, hypertrophic, and hypertensive responses in spontaneously hypertensive rats,” Hypertension, vol. 56, no. 3, pp. 437–444, 2010. View at Publisher · View at Google Scholar · View at Scopus
  44. P. Lacolley, V. Regnault, A. Nicoletti et al., “The vascular smooth muscle cell in arterial pathology: a cell that can take on multiple roles,” Cardiovascular Research, vol. 95, no. 2, pp. 194–204, 2012. View at Publisher · View at Google Scholar
  45. X. Xu, C.-H. Ha, C. Wong et al., “Angiotensin II stimulates protein kinase D-dependent histone deacetylase 5 phosphorylation and nuclear export leading to vascular smooth muscle cell hypertrophy,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 11, pp. 2355–2362, 2007. View at Publisher · View at Google Scholar · View at Scopus
  46. H. Li, W. Li, A. K. Gupta, P. J. Mohler, M. E. Anderson, and I. M. Grumbach, “Calmodulin kinase II is required for angiotensin II-mediated vascular smooth muscle hypertrophy,” American Journal of Physiology, vol. 298, no. 2, pp. H688–H698, 2010. View at Publisher · View at Google Scholar · View at Scopus
  47. M. Okada, T. Usui, W. Mizuno et al., “HDAC4 mediates development of hypertension via vascular inflammation in spontaneous hypertensive rats,” American Journal of Physiology, vol. 302, no. 9, pp. H1894–H1904, 2012. View at Publisher · View at Google Scholar · View at Scopus
  48. G. H. Kim, J. J. Ryan, G. Marsboom et al., “Epigenetic mechanisms of pulmonary hypertension,” Pulmonary Circulation, vol. 1, no. 3, pp. 347–356, 2011. View at Publisher · View at Google Scholar
  49. X. F. Xu, Y. Lv, W. Z. Gu et al., “Epigenetics of hypoxic pulmonary arterial hypertension following intrauterine growth retardation rat: epigenetics in PAH following IUGR,” Respiratory Research, vol. 14, no. 1, article 20, 2013. View at Publisher · View at Google Scholar
  50. L. Zhao, C. N. Chen, N. Hajji et al., “Histone deacetylation inhibition in pulmonary hypertension: therapeutic potential of valproic acid and suberoylanilide hydroxamic acid,” Circulation, vol. 126, no. 4, pp. 455–467, 2012. View at Google Scholar
  51. M. Li, S. R. Riddle, M. G. Frid et al., “Emergence of fibroblasts with a proinflammatory epigenetically altered phenotype in severe hypoxic pulmonary hypertension,” The Journal of Immunology, vol. 187, no. 5, pp. 2711–2722, 2011. View at Publisher · View at Google Scholar · View at Scopus
  52. M. A. Cavasin, K. Demos-Davies, T. R. Horn et al., “Selective class I histone deacetylase inhibition suppresses hypoxia-induced cardiopulmonary remodeling through an antiproliferative mechanism,” Circulation Research, vol. 110, no. 5, pp. 739–748, 2012. View at Publisher · View at Google Scholar · View at Scopus
  53. T. Shimosawa, “Hypertension and its related organ damage—pathophysiology and new diagnostic strategy,” The Japanese Journal of Clinical Pathology, vol. 61, no. 3, pp. 263–270, 2013. View at Google Scholar
  54. P. Libby, P. M. Ridker, and G. K. Hansson, “Progress and challenges in translating the biology of atherosclerosis,” Nature, vol. 473, no. 7347, pp. 317–325, 2011. View at Publisher · View at Google Scholar · View at Scopus
  55. R. R. Bruchas, L. de Las Fuentes, R. M. Carney et al., “The St. Louis African American health-heart study: methodology for the study of cardiovascular disease and depression in young-old African Americans,” BMC Cardiovascular Disorders, vol. 13, no. 1, article 66, 2013. View at Publisher · View at Google Scholar
  56. M. A. Reddy and R. Natarajan, “Epigenetic mechanisms in diabetic vascular complications,” Cardiovascular Research, vol. 90, no. 3, pp. 421–429, 2011. View at Publisher · View at Google Scholar · View at Scopus
  57. A. C. Doran, N. Meller, and C. A. McNamara, “Role of smooth muscle cells in the initiation and early progression of atherosclerosis,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 28, no. 5, pp. 812–819, 2008. View at Publisher · View at Google Scholar · View at Scopus
  58. I. Manabe and G. K. Owens, “Recruitment of serum response factor and hyperacetylation of histones at smooth muscle-specific regulatory regions during differentiation of a novel P19-derived in vitro smooth muscle differentiation system,” Circulation Research, vol. 88, no. 11, pp. 1127–1134, 2001. View at Google Scholar · View at Scopus
  59. D. Cao, Z. Wang, C.-L. Zhang et al., “Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin,” Molecular and Cellular Biology, vol. 25, no. 1, pp. 364–376, 2005. View at Publisher · View at Google Scholar · View at Scopus
  60. O. G. McDonald, B. R. Wamhoff, M. H. Hoofnagle, and G. K. Owens, “Control of SRF binding to CArG box chromatin regulates smooth muscle gene expression in vivo,” The Journal of Clinical Investigation, vol. 116, no. 1, pp. 36–48, 2006. View at Publisher · View at Google Scholar · View at Scopus
  61. J.-H. Choi, K.-H. Nam, J. Kim et al., “Trichostatin A exacerbates atherosclerosis in low density lipoprotein receptor-deficient mice,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 25, no. 11, pp. 2404–2409, 2005. View at Publisher · View at Google Scholar · View at Scopus
  62. S. V. Lakshmi, S. M. Naushad, C. A. Reddy et al., “Oxidative stress in coronary artery disease: epigenetic perspective,” Molecular and Cellular Biochemistry, vol. 374, no. 1-2, pp. 203–211, 2013. View at Publisher · View at Google Scholar
  63. M. Mangino and T. Spector, “Understanding coronary artery disease using twin studies,” Heart, vol. 99, no. 6, pp. 373–375, 2013. View at Publisher · View at Google Scholar
  64. S. M. Nadtochiy, E. Redman, I. Rahman, and P. S. Brookes, “Lysine deacetylation in ischaemic preconditioning: the role of SIRT1,” Cardiovascular Research, vol. 89, no. 3, pp. 643–649, 2011. View at Publisher · View at Google Scholar · View at Scopus
  65. R. J. Wierda, S. B. Geutskens, J. W. Jukema, P. H. A. Quax, and P. J. van den Elsen, “Epigenetics in atherosclerosis and inflammation,” Journal of Cellular and Molecular Medicine, vol. 14, no. 6A, pp. 1225–1240, 2010. View at Publisher · View at Google Scholar · View at Scopus
  66. J. J. V. McMurray and M. A. Pfeffer, “Heart failure,” The Lancet, vol. 365, no. 9474, pp. 1877–1889, 2005. View at Publisher · View at Google Scholar · View at Scopus
  67. I. Kehat and J. D. Molkentin, “Molecular pathways underlying cardiac remodeling during pathophysiological stimulation,” Circulation, vol. 122, no. 25, pp. 2727–2735, 2010. View at Publisher · View at Google Scholar · View at Scopus
  68. R. Gusterson, B. Brar, D. Faulkes, A. Giordano, J. Chrivia, and D. Latchman, “The transcriptional co-activators CBP and p300 are activated via phenylephrine through the p42/p44 MAPK cascade,” The Journal of Biological Chemistry, vol. 277, no. 4, pp. 2517–2524, 2002. View at Publisher · View at Google Scholar · View at Scopus
  69. R. J. Gusterson, E. Jazrawi, I. M. Adcock, and D. S. Latchman, “The transcriptional co-activators CREB-binding protein (CBP) and p300 play a critical role in cardiac hypertrophy that is dependent on their histone acetyltransferase activity,” The Journal of Biological Chemistry, vol. 278, no. 9, pp. 6838–6847, 2003. View at Publisher · View at Google Scholar · View at Scopus
  70. T. Yanazume, K. Hasegawa, T. Morimoto et al., “Cardiac p300 is involved in myocyte growth with decompensated heart failure,” Molecular and Cellular Biology, vol. 23, no. 10, pp. 3593–3606, 2003. View at Publisher · View at Google Scholar · View at Scopus
  71. Y.-S. Dai and B. E. Markham, “p300 functions as a coactivator of transcription factor GATA-4,” The Journal of Biological Chemistry, vol. 276, no. 40, pp. 37178–37185, 2001. View at Publisher · View at Google Scholar · View at Scopus
  72. T. I. Slepak, K. A. Webster, J. Zang et al., “Control of cardiac-specific transcription by p300 through myocyte enhancer factor-2D,” The Journal of Biological Chemistry, vol. 276, no. 10, pp. 7575–7585, 2001. View at Publisher · View at Google Scholar · View at Scopus
  73. D. Cao, C. Wang, R. Tang et al., “Acetylation of myocardin is required for the activation of cardiac and smooth muscle genes,” The Journal of Biological Chemistry, vol. 287, no. 46, pp. 38495–38504, 2012. View at Publisher · View at Google Scholar
  74. C. Colussi, B. Illi, J. Rosati et al., “Histone deacetylase inhibitors: keeping momentum for neuromuscular and cardiovascular diseases treatment,” Pharmacological Research, vol. 62, no. 1, pp. 3–10, 2010. View at Publisher · View at Google Scholar · View at Scopus
  75. D. Dingar, F. Konecny, J. Zou et al., “Anti-apoptotic function of the E2F transcription factor 4 (E2F4)/p130, a member of retinoblastoma gene family in cardiac myocytes,” Journal of Molecular and Cellular Cardiology, vol. 53, no. 6, pp. 820–828, 2012. View at Publisher · View at Google Scholar
  76. K. Tomita, P. J. Barnes, and I. M. Adcock, “The effect of oxidative stress on histone acetylation and IL-8 release,” Biochemical and Biophysical Research Communications, vol. 301, no. 2, pp. 572–577, 2003. View at Publisher · View at Google Scholar · View at Scopus
  77. R. Dooley, B. J. Harvey, and W. Thomas, “The regulation of cell growth and survival by aldosterone,” Frontiers in Bioscience, vol. 16, no. 2, pp. 440–457, 2011. View at Publisher · View at Google Scholar · View at Scopus
  78. A. Planavila, E. Dominguez, M. Navarro et al., “Dilated cardiomyopathy and mitochondrial dysfunction in Sirt1-deficient mice: a role for Sirt1-Mef2 in adult heart,” Journal of Molecular and Cellular Cardiology, vol. 53, no. 4, pp. 521–531, 2012. View at Google Scholar
  79. O. Vakhrusheva, C. Smolka, P. Gajawada et al., “Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis and inflammatory cardiomyopathy in mice,” Circulation Research, vol. 102, no. 6, pp. 703–710, 2008. View at Publisher · View at Google Scholar · View at Scopus
  80. S. S. H. Chen, A. J. Jenkins, and H. Majewski, “Elevated plasma prostaglandins and acetylated histone in monocytes in type 1 diabetes patients,” Diabetic Medicine, vol. 26, no. 2, pp. 182–186, 2009. View at Publisher · View at Google Scholar · View at Scopus
  81. F. Paneni, P. Mocharla, A. Akhmedov et al., “Gene silencing of the mitochondrial adaptor p66Shc suppresses vascular hyperglycemic memory in diabetes,” Circulation Research, vol. 111, no. 3, pp. 278–289, 2012. View at Publisher · View at Google Scholar
  82. X.-Y. Yu, Y.-J. Geng, J.-L. Liang et al., “High levels of glucose induce apoptosis in cardiomyocyte via epigenetic regulation of the insulin-like growth factor receptor,” Experimental Cell Research, vol. 316, no. 17, pp. 2903–2909, 2010. View at Publisher · View at Google Scholar · View at Scopus
  83. H. J. Kee and H. Kook, “Roles and targets of class I and IIa histone deacetylases in cardiac hypertrophy,” Journal of Biomedicine and Biotechnology, vol. 2011, Article ID 928326, 10 pages, 2011. View at Publisher · View at Google Scholar · View at Scopus
  84. R. L. Montgomery, C. A. Davis, M. J. Potthoff et al., “Histone deacetylases 1 and 2 redundantly regulate cardiac morphogenesis, growth, and contractility,” Genes & Development, vol. 21, no. 14, pp. 1790–1802, 2007. View at Publisher · View at Google Scholar · View at Scopus
  85. C. M. Trivedi, Y. Luo, Z. Yin et al., “Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3β activity,” Nature Medicine, vol. 13, no. 3, pp. 324–331, 2007. View at Publisher · View at Google Scholar · View at Scopus
  86. C. M. Trivedi, M. M. Lu, Q. Wang, and J. A. Epstein, “Transgenic overexpression of Hdac3 in the heart produces increased postnatal cardiac myocyte proliferation but does not induce hypertrophy,” The Journal of Biological Chemistry, vol. 283, no. 39, pp. 26484–26489, 2008. View at Publisher · View at Google Scholar · View at Scopus
  87. N. Singh, C. M. Trivedi, M. Lu, S. E. Mullican, M. A. Lazar, and J. A. Epstein, “Histone deacetylase 3 regulates smooth muscle differentiation in neural crest cells and development of the cardiac outflow tract,” Circulation Research, vol. 109, no. 11, pp. 1240–1249, 2011. View at Publisher · View at Google Scholar · View at Scopus
  88. H. J. Kee, E. H. Bae, S. Park et al., “HDAC inhibition suppresses cardiac hypertrophy and fibrosis in DOCA-salt hypertensive rats via regulation of HDAC6/HDAC8 enzyme activity,” Kidney & Blood Pressure Research, vol. 37, no. 4-5, pp. 229–239, 2013. View at Publisher · View at Google Scholar
  89. J. Backs and E. N. Olson, “Control of cardiac growth by histone acetylation/deacetylation,” Circulation Research, vol. 98, no. 1, pp. 15–24, 2006. View at Publisher · View at Google Scholar · View at Scopus
  90. T. A. McKinsey, C. L. Zhang, and E. N. Olson, “MEF2: a calcium-dependent regulator of cell division, differentiation and death,” Trends in Biochemical Sciences, vol. 27, no. 1, pp. 40–47, 2002. View at Publisher · View at Google Scholar · View at Scopus
  91. J. Backs, K. Song, S. Bezprozvannaya, S. Chang, and E. N. Olson, “CaM kinase II selectively signals to histone deacetylase 4 during cardiomyocyte hypertrophy,” The Journal of Clinical Investigation, vol. 116, no. 7, pp. 1853–1864, 2006. View at Publisher · View at Google Scholar · View at Scopus
  92. E. Bush, J. Fielitz, L. Melvin et al., “A small molecular activator of cardiac hypertrophy uncovered in a chemical screen for modifiers of the calcineurin signaling pathway,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 9, pp. 2870–2875, 2004. View at Publisher · View at Google Scholar · View at Scopus
  93. R. B. Vega, B. C. Harrison, E. Meadows et al., “Protein kinases C and D mediate agonist-dependent cardiac hypertrophy through nuclear export of histone deacetylase 5,” Molecular and Cellular Biology, vol. 24, no. 19, pp. 8374–8385, 2004. View at Publisher · View at Google Scholar · View at Scopus
  94. J. Ye, M. Llorian, M. Cardona et al., “A pathway involving HDAC5, cFLIP and caspases regulates expression of the splicing regulator polypyrimidine tract binding protein in the heart,” Journal of Cell Science, vol. 126, part 7, pp. 1682–1691, 2013. View at Publisher · View at Google Scholar
  95. C. L. Zhang, T. A. McKinsey, S. Chang, C. L. Antos, J. A. Hill, and E. N. Olson, “Class II histone deacetylases act as signal-responsive repressors of cardiac hypertrophy,” Cell, vol. 110, no. 4, pp. 479–488, 2002. View at Publisher · View at Google Scholar · View at Scopus
  96. S. Chang, T. A. McKinsey, C. L. Zhang, J. A. Richardson, J. A. Hill, and E. N. Olson, “Histone deacetylases 5 and 9 govern responsiveness of the heart to a subset of stress signals and play redundant roles in heart development,” Molecular and Cellular Biology, vol. 24, no. 19, pp. 8467–8476, 2004. View at Publisher · View at Google Scholar · View at Scopus
  97. L. Chen, A. Endler, and F. Shibasaki, “Hypoxia and angiogenesis: regulation of hypoxia-inducible factors via novel binding factors,” Experimental & Molecular Medicine, vol. 41, no. 12, pp. 849–857, 2009. View at Publisher · View at Google Scholar · View at Scopus
  98. M. To, S. Yamamura, K. Akashi et al., “Defect of adaptation to hypoxia in patients with COPD due to reduction of histone deacetylase 7,” Chest, vol. 141, no. 5, pp. 1233–1242, 2012. View at Publisher · View at Google Scholar · View at Scopus
  99. S. A. Hunt, “ACC/AHA 2005 guideline update for the diagnosis and management of chronic heart failure in the adult: a report of the American College of Cardiology/American Heart Association Task Force on Practice Guidelines (Writing Committee to Update the 2001 Guidelines for the Evaluation and Management of Heart Failure),” Journal of the American College of Cardiology, vol. 46, no. 6, pp. e1–e82, 2005. View at Publisher · View at Google Scholar
  100. S. Udali, P. Guarini, S. Moruzzi et al., “Cardiovascular epigenetics: from DNA methylation to microRNAs,” Molecular Aspects of Medicine, vol. 34, no. 4, pp. 883–901, 2013. View at Publisher · View at Google Scholar
  101. I. K. Sundar, S. Caito, H. Yao, and I. Rahman, “Oxidative stress, thiol redox signaling methods in epigenetics,” Methods in Enzymology, vol. 474, pp. 213–244, 2010. View at Google Scholar · View at Scopus
  102. O. Ozden, S.-H. Park, H.-S. Kim et al., “Acetylation of MnSOD directs enzymatic activity responding to cellular nutrient status or oxidative stress,” Aging, vol. 3, no. 2, pp. 102–107, 2011. View at Google Scholar · View at Scopus
  103. V. Di Stefano, S. Soddu, A. Sacchi, and G. D'Orazi, “HIPK2 contributes to PCAF-mediated p53 acetylation and selective transactivation of p21Waf1 after nonapoptotic DNA damage,” Oncogene, vol. 24, no. 35, pp. 5431–5442, 2005. View at Publisher · View at Google Scholar · View at Scopus
  104. G. Bossis and F. Melchior, “Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes,” Molecular Cell, vol. 21, no. 3, pp. 349–357, 2006. View at Publisher · View at Google Scholar · View at Scopus
  105. S. Yan, X. Sun, B. Xiang et al., “Redox regulation of the stability of the SUMO protease SENP3 via interactions with CHIP and Hsp90,” The EMBO Journal, vol. 29, no. 22, pp. 3773–3786, 2010. View at Publisher · View at Google Scholar · View at Scopus
  106. L. de la Vega, I. Grishina, R. Moreno, M. Krüger, T. Braun, and M. L. Schmitz, “A redox-regulated SUMO/acetylation switch of HIPK2 controls the survival threshold to oxidative stress,” Molecular Cell, vol. 46, no. 4, pp. 472–483, 2012. View at Publisher · View at Google Scholar · View at Scopus
  107. Y. Chen, J. Zhang, Y. Lin et al., “Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS,” EMBO Reports, vol. 12, no. 6, pp. 534–541, 2011. View at Publisher · View at Google Scholar · View at Scopus
  108. J. M. Zimmet and J. M. Hare, “Nitroso-redox interactions in the cardiovascular system,” Circulation, vol. 114, no. 14, pp. 1531–1544, 2006. View at Publisher · View at Google Scholar · View at Scopus
  109. T. Ago, T. Liu, P. Zhai et al., “A redox-dependent pathway for regulating class II HDACs and cardiac hypertrophy,” Cell, vol. 133, no. 6, pp. 978–993, 2008. View at Publisher · View at Google Scholar · View at Scopus
  110. S. Matsushima, J. Kuroda, T. Ago et al., “Increased oxidative stress in the nucleus caused by Nox4 mediates oxidation of HDAC4 and cardiac hypertrophy,” Circulation Research, vol. 112, no. 4, pp. 651–663, 2013. View at Publisher · View at Google Scholar
  111. Q. Wu, W. Xu, L. Cao et al., “SAHA treatment reveals the link between histone lysine acetylation and proteome in nonsmall cell lung cancer A549 cells,” Journal of Proteome Research, vol. 12, no. 9, pp. 4064–4073, 2013. View at Publisher · View at Google Scholar
  112. L. Bossaller and A. Rothe, “Monoclonal antibody treatments for rheumatoid arthritis,” Expert Opinion on Biological Therapy, vol. 13, no. 9, pp. 1257–1272, 2013. View at Google Scholar
  113. K. Zhang, M. Schrag, A. Crofton et al., “Targeted proteomics for quantification of histone acetylation in Alzheimer's disease,” Proteomics, vol. 12, no. 8, pp. 1261–1268, 2012. View at Google Scholar
  114. L. Lv, Y.-P. Tang, X. Han, X. Wang, and Q. Dong, “Therapeutic application of histone deacetylase inhibitors for stroke,” Central Nervous System Agents in Medicinal Chemistry, vol. 11, no. 2, pp. 138–149, 2011. View at Google Scholar · View at Scopus